1ndp
From Proteopedia
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|PDB= 1ndp |SIZE=350|CAPTION= <scene name='initialview01'>1ndp</scene>, resolution 2.2Å | |PDB= 1ndp |SIZE=350|CAPTION= <scene name='initialview01'>1ndp</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
- | |ACTIVITY= [http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] </span> |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ndp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ndp OCA], [http://www.ebi.ac.uk/pdbsum/1ndp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ndp RCSB]</span> | ||
}} | }} | ||
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[[Category: Morera, S.]] | [[Category: Morera, S.]] | ||
[[Category: Veron, M.]] | [[Category: Veron, M.]] | ||
- | [[Category: ADP]] | ||
- | [[Category: MG]] | ||
[[Category: phosphotransferase]] | [[Category: phosphotransferase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:28:57 2008'' |
Revision as of 19:28, 30 March 2008
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, resolution 2.2Å | |||||||
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Ligands: | , | ||||||
Activity: | Nucleoside-diphosphate kinase, with EC number 2.7.4.6 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
ADENOSINE 5'-DIPHOSPHATE BINDING AND THE ACTIVE SITE OF NUCLEOSIDE DIPHOSPHATE KINASE
Overview
The X-ray structure of nucleoside diphosphate kinase (NDP kinase) from the slime mold Dictyostelium discoideum has been determined to 2.2-A resolution and refined to an R-factor of 0.19 with and without bound ADP-Mg2+. The nucleotide binds near His 122, a residue which becomes phosphorylated during the catalytic cycle. The mode of binding is different from that observed in other phosphokinases, and it involves no glycine-rich sequence. The adenine base makes only nonpolar contacts with the protein. It points outside, explaining the lack of specificity of NDP kinase toward the base. The ribose 2'- and 3'-hydroxyls and the pyrophosphate moiety are H-bonded to polar side chains. A Mg2+ ion bridges the alpha- to the beta-phosphate which approaches the imidazole group of His 122 from the N delta side. The geometry at the active site in the ADP-Mg2+ complex suggests a mechanism for catalysis whereby the gamma-phosphate of a nucleoside triphosphate can be transferred onto His 122 with a minimum of atomic motion.
About this Structure
1NDP is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.
Reference
Adenosine 5'-diphosphate binding and the active site of nucleoside diphosphate kinase., Morera S, Lascu I, Dumas C, LeBras G, Briozzo P, Veron M, Janin J, Biochemistry. 1994 Jan 18;33(2):459-67. PMID:8286376
Page seeded by OCA on Sun Mar 30 22:28:57 2008